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Pesquisa : D12.776.476.024.414 [Categoria DeCS]
Referências encontradas : 361 [refinar]
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[PMID]:28947615
[Au] Autor:Kawai T; Takayanagi T; Forrester SJ; Preston KJ; Obama T; Tsuji T; Kobayashi T; Boyer MJ; Cooper HA; Kwok HF; Hashimoto T; Scalia R; Rizzo V; Eguchi S
[Ad] Endereço:From the Cardiovascular Research Center, Department of Physiology, Lewis Katz School of Medicine at Temple University, Philadelphia, PA (T. Kawai, T. Takayanagi, S.J.F., K.J.P., T.O., T. Tsuji, T. Kobayashi, M.J.B., H.A.C., R.S., V.R., S.E.); Faculty of Health Sciences, Macau Special Administrative
[Ti] Título:Vascular ADAM17 (a Disintegrin and Metalloproteinase Domain 17) Is Required for Angiotensin II/ß-Aminopropionitrile-Induced Abdominal Aortic Aneurysm.
[So] Source:Hypertension;70(5):959-963, 2017 Nov.
[Is] ISSN:1524-4563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Angiotensin II (AngII)-activated epidermal growth factor receptor has been implicated in abdominal aortic aneurysm (AAA) development. In vascular smooth muscle cells (VSMCs), AngII activates epidermal growth factor receptor via a metalloproteinase, ADAM17 (a disintegrin and metalloproteinase domain 17). We hypothesized that AngII-dependent AAA development would be prevented in mice lacking ADAM17 in VSMCs. To test this concept, control and VSMC ADAM17-deficient mice were cotreated with AngII and a lysyl oxidase inhibitor, ß-aminopropionitrile, to induce AAA. We found that 52.4% of control mice did not survive because of aortic rupture. All other surviving control mice developed AAA and demonstrated enhanced expression of ADAM17 in the AAA lesions. In contrast, all AngII and ß-aminopropionitrile-treated VSMC ADAM17-deficient mice survived and showed reduction in external/internal diameters (51%/28%, respectively). VSMC ADAM17 deficiency was associated with lack of epidermal growth factor receptor activation, interleukin-6 induction, endoplasmic reticulum/oxidative stress, and matrix deposition in the abdominal aorta of treated mice. However, both VSMC ADAM17-deficient and control mice treated with AngII and ß-aminopropionitrile developed comparable levels of hypertension. Treatment of C57Bl/6 mice with an ADAM17 inhibitory antibody but not with control IgG also prevented AAA development. In conclusion, VSMC ADAM17 silencing or systemic ADAM17 inhibition seems to protect mice from AAA formation. The mechanism seems to involve suppression of epidermal growth factor receptor activation.
[Mh] Termos MeSH primário: Proteína ADAM17
Aminopropionitrilo/metabolismo
Angiotensina II/metabolismo
Aneurisma da Aorta Abdominal
Hipertensão
Músculo Liso Vascular
[Mh] Termos MeSH secundário: Proteína ADAM17/antagonistas & inibidores
Proteína ADAM17/metabolismo
Animais
Aorta Abdominal/metabolismo
Aorta Abdominal/patologia
Aneurisma da Aorta Abdominal/etiologia
Aneurisma da Aorta Abdominal/metabolismo
Aneurisma da Aorta Abdominal/patologia
Aneurisma da Aorta Abdominal/prevenção & controle
Hipertensão/etiologia
Hipertensão/metabolismo
Hipertensão/prevenção & controle
Camundongos
Camundongos Endogâmicos C57BL
Músculo Liso Vascular/metabolismo
Músculo Liso Vascular/patologia
Proteína-Lisina 6-Oxidase/metabolismo
Proteínas Modificadoras da Atividade de Receptores/metabolismo
Receptor do Fator de Crescimento Epidérmico/metabolismo
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptor Activity-Modifying Proteins); 11128-99-7 (Angiotensin II); 151-18-8 (Aminopropionitrile); EC 1.4.3.13 (Protein-Lysine 6-Oxidase); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 3.4.24.86 (ADAM17 Protein); EC 3.4.24.86 (Adam17 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE
[do] DOI:10.1161/HYPERTENSIONAHA.117.09822


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[PMID]:28705698
[Au] Autor:Woolley MJ; Reynolds CA; Simms J; Walker CS; Mobarec JC; Garelja ML; Conner AC; Poyner DR; Hay DL
[Ad] Endereço:Institute of Clinical Sciences, University of Birmingham, Edgbaston, Birmingham, UK.
[Ti] Título:Receptor activity-modifying protein dependent and independent activation mechanisms in the coupling of calcitonin gene-related peptide and adrenomedullin receptors to Gs.
[So] Source:Biochem Pharmacol;142:96-110, 2017 Oct 15.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Calcitonin gene-related peptide (CGRP) or adrenomedullin (AM) receptors are heteromers of the calcitonin receptor-like receptor (CLR), a class B G protein-coupled receptor, and one of three receptor activity-modifying proteins (RAMPs). How CGRP and AM activate CLR and how this process is modulated by RAMPs is unclear. We have defined how CGRP and AM induce Gs-coupling in CLR-RAMP heteromers by measuring the effect of targeted mutagenesis in the CLR transmembrane domain on cAMP production, modeling the active state conformations of CGRP and AM receptors in complex with the Gs C-terminus and conducting molecular dynamics simulations in an explicitly hydrated lipidic bilayer. The largest effects on receptor signaling were seen with H295A , I298A , L302A , N305A , L345A and E348A , F349A and H374A (class B numbering in superscript). Many of these residues are likely to form part of a group in close proximity to the peptide binding site and link to a network of hydrophilic and hydrophobic residues, which undergo rearrangements to facilitate Gs binding. Residues closer to the extracellular loops displayed more pronounced RAMP or ligand-dependent effects. Mutation of H374 to alanine increased AM potency 100-fold in the CGRP receptor. The molecular dynamics simulation showed that TM5 and TM6 pivoted around TM3. The data suggest that hydrophobic interactions are more important for CLR activation than other class B GPCRs, providing new insights into the mechanisms of activation of this class of receptor. Furthermore the data may aid in the understanding of how RAMPs modulate the signaling of other class B GPCRs.
[Mh] Termos MeSH primário: Peptídeo Relacionado com Gene de Calcitonina/metabolismo
Proteína Semelhante a Receptor de Calcitonina/metabolismo
Subunidades alfa Gs de Proteínas de Ligação ao GTP/metabolismo
Proteínas Modificadoras da Atividade de Receptores/metabolismo
Receptores de Adrenomedulina/metabolismo
[Mh] Termos MeSH secundário: Animais
Células COS
Peptídeo Relacionado com Gene de Calcitonina/química
Peptídeo Relacionado com Gene de Calcitonina/genética
Proteína Semelhante a Receptor de Calcitonina/química
Proteína Semelhante a Receptor de Calcitonina/genética
Cercopithecus aethiops
AMP Cíclico/metabolismo
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Simulação de Dinâmica Molecular
Mutação
Ligação Proteica
Ensaio Radioligante
Proteínas Modificadoras da Atividade de Receptores/química
Proteínas Modificadoras da Atividade de Receptores/genética
Receptores de Adrenomedulina/química
Receptores de Adrenomedulina/genética
Proteínas Recombinantes de Fusão
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcitonin Receptor-Like Protein); 0 (Receptor Activity-Modifying Proteins); 0 (Receptors, Adrenomedullin); 0 (Recombinant Fusion Proteins); 83652-28-2 (Calcitonin Gene-Related Peptide); E0399OZS9N (Cyclic AMP); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gs)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE


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[PMID]:28062302
[Au] Autor:Sekiguchi T; Shiraishi A; Satake H; Kuwasako K; Takahashi H; Sato M; Urata M; Wada S; Endo M; Ikari T; Hattori A; Srivastav AK; Suzuki N
[Ad] Endereço:Noto Marine Laboratory, Institute of Nature and Environmental Technology, Division of Marine Environmental Studies, Kanazawa University, Housu-gun, Ishikawa 927-0553, Japan.
[Ti] Título:Calcitonin-typical suppression of osteoclastic activity by amphioxus calcitonin superfamily peptides and insights into the evolutionary conservation and diversity of their structures.
[So] Source:Gen Comp Endocrinol;246:294-300, 2017 May 15.
[Is] ISSN:1095-6840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Calcitonin (CT) is a hormone that decreases serum calcium level by suppressing osteoclastic activity in the vertebrate bone. In vertebrates, the structure-function relationship of CTs has been studied extensively. We recently identified three CT superfamily peptides, Bf-CTFP1 to 3, and clarified the molecular and functional characteristics of their receptor and receptor activity-modifying protein in amphioxus, Branchiostoma floridae. However, the CT activity of Bf-CTFPs has yet to be investigated. In the present study, a functional analysis of Bf-CTFPs was performed using goldfish scales having both osteoclasts and osteoblasts. All Bf-CTFPs suppressed osteoclastic activity via a goldfish CT receptor. Although the primary amino acid sequences of the Bf-CTFPs showed low sequence similarity to vertebrate CTs, Bf-CTFP1 to 3 share three amino acids, Thr , Thr , and Pro -NH , that are required for receptor binding, with salmon CT. Moreover, homology model analysis revealed that the Bf-CTFPs form alpha-helical structures. The alpha-helical position and length of Bf-CTFP1 and 2 were conserved with those of a highly potent ligand, teleost CT. Interestingly, the composition of the alpha-helix of Bf-CTFP3 differed from those of teleost CT, despite that the action of Bf-CTFP3 on goldfish scales was the same as that of Bf-CTFP1 and 2. Collectively, the present study provides new insights into the structure-function relationship of CT and its functional evolution in chordates.
[Mh] Termos MeSH primário: Calcitonina/genética
Carpa Dourada/metabolismo
Peptídeos/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas Modificadoras da Atividade de Receptores/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Receptor Activity-Modifying Proteins); 9007-12-9 (Calcitonin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170512
[Lr] Data última revisão:
170512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE


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[PMID]:27106110
[Au] Autor:Novoselova TV; Larder R; Rimmington D; Lelliott C; Wynn EH; Gorrigan RJ; Tate PH; Guasti L; O'Rahilly S; Clark AJ; Logan DW; Coll AP; Chan LF; Sanger Mouse Genetics Project
[Ad] Endereço:Centre for EndocrinologyQueen Mary University of London, William Harvey Research Institute, Barts and the London School of Medicine and Dentistry, Charterhouse Square, London, UK.
[Ti] Título:Loss of Mrap2 is associated with Sim1 deficiency and increased circulating cholesterol.
[So] Source:J Endocrinol;230(1):13-26, 2016 Jul.
[Is] ISSN:1479-6805
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Melanocortin receptor accessory protein 2 (MRAP2) is a transmembrane accessory protein predominantly expressed in the brain. Both global and brain-specific deletion of Mrap2 in mice results in severe obesity. Loss-of-function MRAP2 mutations have also been associated with obesity in humans. Although MRAP2 has been shown to interact with MC4R, a G protein-coupled receptor with an established role in energy homeostasis, appetite regulation and lipid metabolism, the mechanisms through which loss of MRAP2 causes obesity remains uncertain. In this study, we used two independently derived lines of Mrap2 deficient mice (Mrap2(tm1a/tm1a)) to further study the role of Mrap2 in the regulation of energy balance and peripheral lipid metabolism. Mrap2(tm1a/tm1a) mice have a significant increase in body weight, with increased fat and lean mass, but without detectable changes in food intake or energy expenditure. Transcriptomic analysis showed significantly decreased expression of Sim1, Trh, Oxt and Crh within the hypothalamic paraventricular nucleus of Mrap2(tm1a/tm1a) mice. Circulating levels of both high-density lipoprotein and low-density lipoprotein were significantly increased in Mrap2 deficient mice. Taken together, these data corroborate the role of MRAP2 in metabolic regulation and indicate that, at least in part, this may be due to defective central melanocortin signalling.
[Mh] Termos MeSH primário: Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Colesterol/sangue
Metabolismo Energético/genética
Proteínas Modificadoras da Atividade de Receptores/metabolismo
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Animais
Ansiedade/genética
Ansiedade/metabolismo
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Comportamento Animal/fisiologia
Peso Corporal/genética
Hormônio Liberador da Corticotropina/genética
Hormônio Liberador da Corticotropina/metabolismo
Ingestão de Alimentos/genética
Metabolismo dos Lipídeos/genética
Camundongos
Camundongos Knockout
Atividade Motora/genética
Neurônios/metabolismo
Ocitocina/genética
Ocitocina/metabolismo
Núcleo Hipotalâmico Paraventricular/metabolismo
Proteínas Modificadoras da Atividade de Receptores/genética
Proteínas Repressoras/genética
Hormônio Liberador de Tireotropina/genética
Hormônio Liberador de Tireotropina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (MRAP2 protein, mouse); 0 (Receptor Activity-Modifying Proteins); 0 (Repressor Proteins); 0 (Sim1 protein, mouse); 50-56-6 (Oxytocin); 5Y5F15120W (Thyrotropin-Releasing Hormone); 9015-71-8 (Corticotropin-Releasing Hormone); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160424
[St] Status:MEDLINE
[do] DOI:10.1530/JOE-16-0057


  5 / 361 MEDLINE  
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[PMID]:27068971
[Au] Autor:Hay DL; Walker CS; Gingell JJ; Ladds G; Reynolds CA; Poyner DR
[Ad] Endereço:School of Biological Sciences, University of Auckland, Auckland 1010, New Zealand DL.Hay@auckland.ac.nz D.R.Poyner@aston.ac.uk.
[Ti] Título:Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins.
[So] Source:Biochem Soc Trans;44(2):568-73, 2016 Apr 15.
[Is] ISSN:1470-8752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Receptor activity-modifying proteins (RAMPs) are single pass membrane proteins initially identified by their ability to determine the pharmacology of the calcitonin receptor-like receptor (CLR), a family B G protein-coupled receptor (GPCR). It is now known that RAMPs can interact with a much wider range of GPCRs. This review considers recent developments on the structure of the complexes formed between the extracellular domains (ECDs) of CLR and RAMP1 or RAMP2 as these provide insights as to how the RAMPs direct ligand binding. The range of RAMP interactions is also considered; RAMPs can interact with numerous family B GPCRs as well as examples of family A and family C GPCRs. They influence receptor expression at the cell surface, trafficking, ligand binding and G protein coupling. The GPCR-RAMP interface offers opportunities for drug targeting, illustrated by examples of drugs developed for migraine.
[Mh] Termos MeSH primário: Proteínas Modificadoras da Atividade de Receptores/metabolismo
Receptores Acoplados a Proteínas-G/metabolismo
[Mh] Termos MeSH secundário: Animais
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Receptor Activity-Modifying Proteins); 0 (Receptors, G-Protein-Coupled)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161231
[Lr] Data última revisão:
161231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160413
[St] Status:MEDLINE
[do] DOI:10.1042/BST20150237


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[PMID]:26829592
[Au] Autor:Chaly AL; Srisai D; Gardner EE; Sebag JA
[Ad] Endereço:Department of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, United States.
[Ti] Título:The Melanocortin Receptor Accessory Protein 2 promotes food intake through inhibition of the Prokineticin Receptor-1.
[So] Source:Elife;5, 2016 Feb 01.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Melanocortin Receptor Accessory Protein 2 (MRAP2) is an important regulator of energy homeostasis and its loss causes severe obesity in rodents. MRAP2 mediates its action in part through the potentiation of the MC4R, however, it is clear that MRAP2 is expressed in tissues that do not express MC4R, and that the deletion of MRAP2 does not recapitulate the phenotype of Mc4r KO mice. Consequently, we hypothesized that other GPCRs involved in the control of energy homeostasis are likely to be regulated by MRAP2. In this study we identified PKR1 as the first non-melanocortin GPCR to be regulated by MRAP2. We show that MRAP2 significantly and specifically inhibits PKR1 signaling. We also demonstrate that PKR1 and MRAP2 co-localize in neurons and that Mrap2 KO mice are hypersensitive to PKR1 stimulation. This study not only identifies new partners of MRAP2 but also a new pathway through which MRAP2 regulates energy homeostasis.
[Mh] Termos MeSH primário: Ingestão de Alimentos
Proteínas Modificadoras da Atividade de Receptores/metabolismo
Receptores Acoplados a Proteínas-G/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Camundongos
Camundongos Knockout
Neurônios/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (MRAP2 protein, mouse); 0 (PKR1 protein, mouse); 0 (Receptor Activity-Modifying Proteins); 0 (Receptors, G-Protein-Coupled)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170125
[Lr] Data última revisão:
170125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160202
[St] Status:MEDLINE


  7 / 361 MEDLINE  
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[PMID]:26740457
[Au] Autor:Klein KR; Matson BC; Caron KM
[Ad] Endereço:a Department of Cell Biology & Physiology and.
[Ti] Título:The expanding repertoire of receptor activity modifying protein (RAMP) function.
[So] Source:Crit Rev Biochem Mol Biol;51(1):65-71, 2016.
[Is] ISSN:1549-7798
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Receptor activity modifying proteins (RAMPs) associate with G-protein-coupled receptors (GPCRs) at the plasma membrane and together bind a variety of peptide ligands, serving as a communication interface between the extracellular and intracellular environments. The collection of RAMP-interacting GPCRs continues to expand and now consists of GPCRs from families A, B and C, suggesting that RAMP activity is extremely prevalent. RAMP association with GPCRs can regulate GPCR function by altering ligand binding, receptor trafficking and desensitization, and downstream signaling pathways. Here, we elaborate on these RAMP-dependent mechanisms of GPCR regulation, which provide opportunities for pharmacological intervention.
[Mh] Termos MeSH primário: Proteínas Modificadoras da Atividade de Receptores/fisiologia
[Mh] Termos MeSH secundário: Ligantes
Filogenia
Ligação Proteica
Proteínas Modificadoras da Atividade de Receptores/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Ligands); 0 (Receptor Activity-Modifying Proteins)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160108
[St] Status:MEDLINE
[do] DOI:10.3109/10409238.2015.1128875


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[PMID]:26644465
[Au] Autor:Sekiguchi T; Kuwasako K; Ogasawara M; Takahashi H; Matsubara S; Osugi T; Muramatsu I; Sasayama Y; Suzuki N; Satake H
[Ad] Endereço:From the Noto Marine Laboratory, Division of Marine Environmental Studies, Institute of Nature and Environmental Technology, Kanazawa University, Housu-gun, Ishikawa 927-0553, Japan, t-sekiguchi@se.kanazawa-u.ac.jp.
[Ti] Título:Evidence for Conservation of the Calcitonin Superfamily and Activity-regulating Mechanisms in the Basal Chordate Branchiostoma floridae: INSIGHTS INTO THE MOLECULAR AND FUNCTIONAL EVOLUTION IN CHORDATES.
[So] Source:J Biol Chem;291(5):2345-56, 2016 Jan 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The calcitonin (CT)/CT gene-related peptide (CGRP) family is conserved in vertebrates. The activities of this peptide family are regulated by a combination of two receptors, namely the calcitonin receptor (CTR) and the CTR-like receptor (CLR), and three receptor activity-modifying proteins (RAMPs). Furthermore, RAMPs act as escort proteins by translocating CLR to the cell membrane. Recently, CT/CGRP family peptides have been identified or inferred in several invertebrates. However, the molecular characteristics and relevant functions of the CTR/CLR and RAMPs in invertebrates remain unclear. In this study, we identified three CT/CGRP family peptides (Bf-CTFPs), one CTR/CLR-like receptor (Bf-CTFP-R), and three RAMP-like proteins (Bf-RAMP-LPs) in the basal chordate amphioxus (Branchiostoma floridae). The Bf-CTFPs were shown to possess an N-terminal circular region typical of the CT/CGRP family and a C-terminal Pro-NH2. The Bf-CTFP genes were expressed in the central nervous system and in endocrine cells of the midgut, indicating that Bf-CTFPs serve as brain and/or gut peptides. Cell surface expression of the Bf-CTFP-R was enhanced by co-expression with each Bf-RAMP-LP. Furthermore, Bf-CTFPs activated Bf-CTFP-R·Bf-RAMP-LP complexes, resulting in cAMP accumulation. These results confirmed that Bf-RAMP-LPs, like vertebrate RAMPs, are prerequisites for the function and translocation of the Bf-CTFP-R. The relative potencies of the three peptides at each receptor were similar. Bf-CTFP2 was a potent ligand at all receptors in cAMP assays. Bf-RAMP-LP effects on ligand potency order were distinct to vertebrate CGRP/adrenomedullin/amylin receptors. To the best of our knowledge, this is the first molecular and functional characterization of an authentic invertebrate CT/CGRP family receptor and RAMPs.
[Mh] Termos MeSH primário: Calcitonina/genética
Calcitonina/metabolismo
Evolução Molecular
Regulação da Expressão Gênica
Anfioxos/metabolismo
Família Multigênica
[Mh] Termos MeSH secundário: Adrenomedulina/metabolismo
Sequência de Aminoácidos
Animais
Células COS
Peptídeo Relacionado com Gene de Calcitonina/metabolismo
Proteína Semelhante a Receptor de Calcitonina/metabolismo
Membrana Celular/metabolismo
Sistema Nervoso Central/metabolismo
Cercopithecus aethiops
Cordados
Clonagem Molecular
AMP Cíclico/metabolismo
Citometria de Fluxo
Células HEK293
Seres Humanos
Intestinos/metabolismo
Polipeptídeo Amiloide das Ilhotas Pancreáticas/metabolismo
Dados de Sequência Molecular
Fases de Leitura Aberta
Filogenia
Estrutura Terciária de Proteína
Proteínas Modificadoras da Atividade de Receptores/metabolismo
Receptores da Calcitonina/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcitonin Receptor-Like Protein); 0 (Islet Amyloid Polypeptide); 0 (Receptor Activity-Modifying Proteins); 0 (Receptors, Calcitonin); 148498-78-6 (Adrenomedullin); 83652-28-2 (Calcitonin Gene-Related Peptide); 9007-12-9 (Calcitonin); E0399OZS9N (Cyclic AMP)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170129
[Lr] Data última revisão:
170129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151209
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.664003


  9 / 361 MEDLINE  
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[PMID]:26514202
[Au] Autor:Hay DL; Pioszak AA
[Ad] Endereço:School of Biological Sciences and Maurice Wilkins Center, University of Auckland, Auckland 1142, New Zealand; email: dl.hay@auckland.ac.nz.
[Ti] Título:Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles.
[So] Source:Annu Rev Pharmacol Toxicol;56:469-87, 2016.
[Is] ISSN:1545-4304
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is now recognized that G protein-coupled receptors (GPCRs), once considered largely independent functional units, have a far more diverse molecular architecture. Receptor activity-modifying proteins (RAMPs) provide an important example of proteins that interact with GPCRs to modify their function. RAMPs are able to act as pharmacological switches and chaperones, and they can regulate signaling and/or trafficking in a receptor-dependent manner. This review covers recent discoveries in the RAMP field and summarizes the known GPCR partners and functions of RAMPs. We also discuss the first peptide-bound structures of RAMP-GPCR complexes, which give insight into the molecular mechanisms that enable RAMPs to alter the pharmacology and signaling of GPCRs.
[Mh] Termos MeSH primário: Proteínas Modificadoras da Atividade de Receptores/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Proteínas de Membrana/metabolismo
Ligação Proteica/fisiologia
Receptores Acoplados a Proteínas-G/metabolismo
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Receptor Activity-Modifying Proteins); 0 (Receptors, G-Protein-Coupled)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151031
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-pharmtox-010715-103120


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[PMID]:26510864
[Au] Autor:Dong Y; Betancourt A; Chauhan M; Balakrishnan M; Lugo F; Anderson ML; Espinoza J; Fox K; Belfort M; Yallampalli C
[Ad] Endereço:Department of Obstetrics and Gynecology, Baylor College of Medicine/Texas Children's Hospital, Houston, Texas.
[Ti] Título:Pregnancy Increases Relaxation in Human Omental Arteries to the CGRP Family of Peptides.
[So] Source:Biol Reprod;93(6):134, 2015 Dec.
[Is] ISSN:1529-7268
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Calcitonin gene-related peptide (CALCB) and its family members adrenomedullin (ADM) and intermedin (ADM2) play important roles in maintaining vascular adaptations during pregnancy in animal models. The present study was designed to evaluate the responses of omental arteries to CALCB, ADM, and ADM2 in pregnant and nonpregnant women, and to determine the mechanisms involved. By using resistance omental arteries collected from nonpregnant women (n = 15) during laparotomy and from term pregnant women (n = 15) at cesarean delivery, this study shows that the receptor components--calcitonin receptor-like receptor (CALCRL) and receptor activity-modifying proteins (RAMPs) 1, 2 and 3--are localized to endothelial and smooth muscle cells in omental arteries, with increased expressions of both mRNA and protein in pregnant compared with nonpregnant women. The myography study demonstrated that CALCB, ADM, and ADM2 (0.1-100 nM) dose dependently relax U46619 (1 muM) precontracted omental artery segments, and the maximum possible effects to CALCB and ADM2, but not to ADM, are significantly enhanced in pregnant compared with nonpregnant women. Further, the vasodilatory responses to CALCB, ADM, and ADM2 are reduced by inhibitors of nitric oxide (NO) synthase (L-NAME), adenylyl cyclase (SQ22536), voltage-activated potassium channels (4-aminopyrodin and tetrabutylammonium), Ca(2+)-activated potassium channel (charybdotoxin), and cyclooxygenase (indomethacin). In conclusion, the CALCB family of peptides, CALCB and ADM2, increase human omental artery relaxation during pregnancy through diverse mechanisms, including NO, endothelium-derived hyperpolarizing factors (EDHFs) and prostaglandins, and thus could contribute to the vascular adaptations during pregnancy in the human.
[Mh] Termos MeSH primário: Adrenomedulina/farmacologia
Artérias/efeitos dos fármacos
Peptídeo Relacionado com Gene de Calcitonina/farmacologia
Omento/irrigação sanguínea
Hormônios Peptídicos/farmacologia
Vasodilatação/efeitos dos fármacos
[Mh] Termos MeSH secundário: Artérias/metabolismo
Proteína Semelhante a Receptor de Calcitonina/metabolismo
Relação Dose-Resposta a Droga
Endotélio Vascular/efeitos dos fármacos
Endotélio Vascular/metabolismo
Feminino
Seres Humanos
Óxido Nítrico/metabolismo
Gravidez
Proteínas Modificadoras da Atividade de Receptores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ADM2 protein, human); 0 (Calcitonin Receptor-Like Protein); 0 (Peptide Hormones); 0 (Receptor Activity-Modifying Proteins); 148498-78-6 (Adrenomedullin); 31C4KY9ESH (Nitric Oxide); 83652-28-2 (Calcitonin Gene-Related Peptide)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151030
[St] Status:MEDLINE
[do] DOI:10.1095/biolreprod.115.135665



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